Purification and Properties of Ornithine Racemase from Clostridium sticklandii
Resource
Journal of Bacteriology 182 (7): 2052-2054
Journal
Journal of Bacteriology
Pages
2052-2054
Date Issued
2000
Date
2000
Author(s)
Chen, Hao-Ping
Lin, Chin-Fen
Lee, Ya-Jung
Tsay, San-San
Wu, Shih-Hsiung
Abstract
Ornithine racemase has been purified to homogeneity from Clostridium sticklandii, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This is the first racemase known to be highly specific to ornithine. This PLP-dependent enzyme has an M(r) of 92, 000, with a K(m) for L-ornithine of 0.77 +/- 0.05 mM and a k(cat) of 980 +/- 20 s(-1).
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